ID C3XU74_BRAFL Unreviewed; 1051 AA.
AC C3XU74;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_121021 {ECO:0000313|EMBL:EEN68448.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN68448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN68448.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN68448.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; GG666464; EEN68448.1; -; Genomic_DNA.
DR RefSeq; XP_002612439.1; XM_002612393.1.
DR AlphaFoldDB; C3XU74; -.
DR eggNOG; ENOG502QS3J; Eukaryota.
DR InParanoid; C3XU74; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 304..565
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 971..1042
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 1051 AA; 116275 MW; 14E63003E0523BE8 CRC64;
MYLLVKLQQG GKRRKREKDA PMALDSAYFN GFAPDGTSVV TRICRRHGRR AEIWFILHVP
GVGVLQAPQH PDTAVFNTDG KTFSAAGLHF EPVEAMRTWK VQFNGLMRLT ESPRTDVTKE
EGRLVHVRFS FMWSAYTLPF NFDTDIHPRA IARAMAIEKW NKQFFQDLRS LRTGYVFTPN
GTMEAVSEVD LVLSSIGEDG TMPDNYSFSF VAGGKKYHVQ VEIYCQSTWY NGLQWESRVH
ERLANFTVNG LKGWGVCEFN YKNTTGCPLP PRESRPQQPL PDITSTHRKL LTLSLSSPVC
RSTELVGGKG SSLVTLTALQ SEGTMFKVPS GFCVTMAAME LQLKLHPTLK SKLEELKQVS
CVGDMFTSVA LAPDVREAIR AELDNLSDSQ FAVRSSAIGE DTEEMSAAGQ MTTELGVRGL
DQICDSVQKC WASLYGFPAV QYRRQHGQPV VSSMAVVVQE MVPAEVAGVL FTQHPVTGHP
GKMVINANYG LGESVVSGDS HPDTITLSGG VDGTCQVEGV DLGSKTQQVV PLDGGGTAVQ
EVASAQSEKC CLSDDTAVQL GHIAVKNIAA SVLSRKCQPY FKKMGLCLGH MFINMHNVAE
IYEHHVAIAD KRVAEMSLVG RHLYTSKHKI HRLEQTLTTY TICRHDNAMA MYQEINERLP
DCYQAWADHM SYGARSAAWS TVLMMVLSRG AREWTMQHFS DMAHFYVNCE QVTSADVPDA
LEKLAVKLIE EGHKDRLIAM SPQDATTWLL GADSGSSGQL FQTFLDLHGH RCLREAELRE
MSWRAAPTKV VLTIQTMLRN NQIASVKESF NFDEAVKKIK SPITMAGKYI LKWTLPYARQ
GVMEREQSKS AAVKMADHFK QAYWYLASLM VAEGRLPEED LLFFLTHQEI GTLLHSRSAV
LVAKALRRRR ILPKQMSLKF PEICRGHPEP IEVGVLNVSG SDLMLKGMPV SHGTVTAPAR
VVTRLEDAGT IQAGEILIVQ STDIGWSPYF PLLSGLVTEL GGLISHGAVV AREYGLPCVV
SVKNATAMFQ TGDMVLLNGT EGSVRKLNPD N
//